Biochemical properties and expression profile of human prolyl dipeptidase DPP9

Hung Kuan Tang; Hsiang Yun Tang; Shu Ching Hsu; Yue Ru Chu; Chia Hui Chien; Chin Hang Shu; Xin Chen

doi:10.1016/j.abb.2009.02.015

Biochemical properties and expression profile of human prolyl dipeptidase DPP9

Hung Kuan Tang, Hsiang Yun Tang, Shu Ching Hsu, Yue Ru Chu, Chia Hui Chien, Chin Hang Shu, Xin Chen

Department of Chemical and Materials Engineering

Research output: Contribution to journal › Article › peer-review

30 Scopus citations

Abstract

Dipetidyl peptidase 9 (DPP9) is a prolyl dipeptidase preferentially cleaving the peptide bond after the penultimate proline residue. The biological function of DPP9 is unknown. In this study, we have significantly improved the yield using Strep·Tactin^® purification system and characterized the biochemical property of DPP9. Moreover, the dimer interaction mode was investigated by introducing a mutation (F842A) at the dimer interface, which abolished the enzymatic activity without disrupting its quaternary structure. Furthermore, DPP9 was found ubiquitously expressed in fibroblasts, epithelial, and blood cells. Surprisingly, contrary to previous report, we found that the expression levels of DPP8 and DPP9 did not change upon the activation of the PBMC or Jurkat cells. These results indicate that the biochemical property of DPP9 is very similar to that of DPP8, its homologous protease. DPP9 and DPP8 are likely redundant proteins carrying out overlapping functions in vivo.

Original language	English
Pages (from-to)	120-127
Number of pages	8
Journal	Archives of Biochemistry and Biophysics
Volume	485
Issue number	2
DOIs	https://doi.org/10.1016/j.abb.2009.02.015
State	Published - 15 May 2009

Keywords

Dimerization
Dipeptidyl peptidase
DPP9
Substrate specificity

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title = "Biochemical properties and expression profile of human prolyl dipeptidase DPP9",

abstract = "Dipetidyl peptidase 9 (DPP9) is a prolyl dipeptidase preferentially cleaving the peptide bond after the penultimate proline residue. The biological function of DPP9 is unknown. In this study, we have significantly improved the yield using Strep·Tactin{\textregistered} purification system and characterized the biochemical property of DPP9. Moreover, the dimer interaction mode was investigated by introducing a mutation (F842A) at the dimer interface, which abolished the enzymatic activity without disrupting its quaternary structure. Furthermore, DPP9 was found ubiquitously expressed in fibroblasts, epithelial, and blood cells. Surprisingly, contrary to previous report, we found that the expression levels of DPP8 and DPP9 did not change upon the activation of the PBMC or Jurkat cells. These results indicate that the biochemical property of DPP9 is very similar to that of DPP8, its homologous protease. DPP9 and DPP8 are likely redundant proteins carrying out overlapping functions in vivo.",

keywords = "Dimerization, Dipeptidyl peptidase, DPP9, Substrate specificity",

author = "Tang, {Hung Kuan} and Tang, {Hsiang Yun} and Hsu, {Shu Ching} and Chu, {Yue Ru} and Chien, {Chia Hui} and Shu, {Chin Hang} and Xin Chen",

note = "Funding Information: We would like to thank Dr. Kuei-Min Chung for the critical reading and comments in the paper, and to Mrs. Wen-Hsing Chen and Mr. Ching-Hsun Kang for their technical assistance. This study was supported financially by National Research Program for Genomic Medicine (NRPGM), National Science Council, Taiwan, and National Health Research Institutes, Taiwan, ROC. ",

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AU - Tang, Hung Kuan

AU - Tang, Hsiang Yun

AU - Hsu, Shu Ching

AU - Chu, Yue Ru

AU - Chien, Chia Hui

AU - Shu, Chin Hang

AU - Chen, Xin

N1 - Funding Information: We would like to thank Dr. Kuei-Min Chung for the critical reading and comments in the paper, and to Mrs. Wen-Hsing Chen and Mr. Ching-Hsun Kang for their technical assistance. This study was supported financially by National Research Program for Genomic Medicine (NRPGM), National Science Council, Taiwan, and National Health Research Institutes, Taiwan, ROC.

PY - 2009/5/15

Y1 - 2009/5/15

N2 - Dipetidyl peptidase 9 (DPP9) is a prolyl dipeptidase preferentially cleaving the peptide bond after the penultimate proline residue. The biological function of DPP9 is unknown. In this study, we have significantly improved the yield using Strep·Tactin® purification system and characterized the biochemical property of DPP9. Moreover, the dimer interaction mode was investigated by introducing a mutation (F842A) at the dimer interface, which abolished the enzymatic activity without disrupting its quaternary structure. Furthermore, DPP9 was found ubiquitously expressed in fibroblasts, epithelial, and blood cells. Surprisingly, contrary to previous report, we found that the expression levels of DPP8 and DPP9 did not change upon the activation of the PBMC or Jurkat cells. These results indicate that the biochemical property of DPP9 is very similar to that of DPP8, its homologous protease. DPP9 and DPP8 are likely redundant proteins carrying out overlapping functions in vivo.

AB - Dipetidyl peptidase 9 (DPP9) is a prolyl dipeptidase preferentially cleaving the peptide bond after the penultimate proline residue. The biological function of DPP9 is unknown. In this study, we have significantly improved the yield using Strep·Tactin® purification system and characterized the biochemical property of DPP9. Moreover, the dimer interaction mode was investigated by introducing a mutation (F842A) at the dimer interface, which abolished the enzymatic activity without disrupting its quaternary structure. Furthermore, DPP9 was found ubiquitously expressed in fibroblasts, epithelial, and blood cells. Surprisingly, contrary to previous report, we found that the expression levels of DPP8 and DPP9 did not change upon the activation of the PBMC or Jurkat cells. These results indicate that the biochemical property of DPP9 is very similar to that of DPP8, its homologous protease. DPP9 and DPP8 are likely redundant proteins carrying out overlapping functions in vivo.

KW - Dimerization

KW - Dipeptidyl peptidase

KW - DPP9

KW - Substrate specificity

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Biochemical properties and expression profile of human prolyl dipeptidase DPP9

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Keywords

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